You searched for: Proteins and Peptides

Supplier: MilliporeSigma

Native α1-acid glycoprotein from human plasma. Glycoprotein used for the study of the structure of oligosaccharide units. Consists of 40 - 45% carbohydrate. Present in human plasma at concentrations of 55 - 140 mg/100 mL. Clinically, α1-AG is an acute-phase reactant that, together with haptoglobin, indicates acute inflammation. Selectively suppresses the augmentation of NK cell activity by IFN-α and IFN-ɣ.

Supplier: MilliporeSigma

Inhibitor of calpain I (Ki=190nM), calpain II (Ki=220nM), cathepsin B (Ki=150nM) and cathepsin L (Ki=0.5nM). Inhibits neutral cysteine proteases and the proteasome (Ki=6µM). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Also inhibits retrovirus-induced apoptosis in L929 cells. Inhibits the proteolysis of I[kappa]B-[alpha] and I[kappa]B-[beta] by the ubiquitin-proteasome complex. Inhibits cell cycle progression at G1/S and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also prevents nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene.

Supplier: Prosci

Secreted Phosphoprotein 1 (SPP1) is a secreted multifunctional glycoprotein. Its putative functions include roles in bone metabolism, immune regulation, wound healing, cell survival, and tumor progression. Based on gene structure and chromosomal location, SPP1 is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family that also includes bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), enamelin (ENAM), and matrix extracellular phosphoglycoprotein (MEPE). SPP1 is expressed in bone, although it is also expressed in other tissues. SPP1 acts as a cytokine that is involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10. It is essential in the pathway that leads to type I immunity. Osteopontin has been implicated as an important factor in bone remodeling. Specifically, research suggests it plays a role in anchoring osteoclasts to the mineral matrix of bones. The fact that SPP1 interacts with multiple cell surface receptors which are ubiquitously expressed makes it an active player in many physiological and pathological processes including wound healing, bone turnover, tumorigenesis, inflammation and ischemia. Therefore, manipulation of plasma Osteopontin levels may be useful in the treatment of autoimmune diseases, cancer metastasis, osteoporosis and some forms of stress.

Supplier: Prosci

CD28 and CTLA-4 together with their ligands, CD80 (B7-1) and CD86 (B7-2), constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD28 and CTLA-4 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD28 and CTLA-4 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. The genes encoding these two molecules are closely linked on human chromosome 2 and mouse chromosome 1. Mouse CD28 is expressed constitutively on virtually 100% of mouse T cells and on developing thymocytes. Cell surface expression of mouse CD28 is downregulated upon ligation of CD28 in the presence of PMA or PHA. In contrast, CTLA-4 is not expressed constitutively but is upregulated rapidly following T cell activation and CD28 ligation. Cell surface expression of mouse CTLA-4 peaks approx.y 48 hours after activation. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28. CD28/B7 interaction has been shown to prevent apoptosis of activated T cells via the upregulation of bcl-XL. CD28 ligation has also been shown to regulate Th1/Th2 differentiation.

Supplier: Prosci

BH3-Interacting Domain Death Agonist (BID) is a member of the Bcl-2 protein family which regulates outer mitochondrial membrane permeability. BID is a pro-apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. Interaction of Bid with Bak causes altered mitochondrial membrane permeability. BID contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. It is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent, and also offer a new strategy for the treatment of acute renal failure associated with ischemia-reperfusion. BID receives direct inputs from a key regulator of the cell cycle arrest/DNA repair machinery (ATM), and therefore is an excellent candidate to coordinate genotoxic stress responses and apoptotic cell death. BID is a novel pro-apoptosis Bcl-2 family protein that is activated by caspase 8 in response to Fas/TNF-R1 death receptor signals. Deletion of BID inhibits carcinogenesis in the liver, although this genetic alteration promotes tumorigenesis in the myeloid cells. This is likely related to the function of BID to promote cell cycle progression into S phase. BID could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint.

Supplier: Prosci

Noggin is also known as NOG?SYM1, SYNS1 and is a secreted homodimeric glycoprotein whose scaffold contains a cystine-knot topology similar to that of BMPs.Secreted Noggin probably remains close to the cell surface due to its binding of heparincontaining proteoglycans.Noggin inhibits TGF-? signal transduction by binding to TGF-? family ligands and preventing them from binding to their corresponding receptors. Noggin plays a key role in neural induction by inhibiting BMP4, along with other TGF-? signaling inhibitors such as chordin and follistatin. Mouse knockout experiments have demonstrated that noggin also plays a crucial role in bone development, joint formation, and neural tube fusion. During embryogenesis, Noggin antagonizes specific BMPs at defined times, for example, during neural tube, somite and cardiomyocyte growth and patterning. During skeletal development, Noggin prevents chondrocyte hyperplasia, thus allowing proper formation of joints. During culture of human embryonic stem cells (hESC) or neural stem cells under certain conditions, addition of Noggin to antagonize BMP activity may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons Noggin also appears to maintain adult stem cell populations in vivo, for example, maintaining neural stem cells within the hippocampus.

Supplier: Prosci

NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.

Supplier: Prosci

Epidermal growth factor (EGF) is a growth factor and the founding member of the EGF family. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. These receptors undergo a complex pattern of ligand induced homo or heterodimerization to transduce EGF family signals. EGF binds to the receptor EGFR stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity initiates a signal transduction cascade that results in a variety of biochemical changes within the cell, including a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR, which lead to DNA synthesis, cell growth, proliferation and differentiation. Other biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.

Supplier: Prosci

Tumor Necrosis Factor- alpha (TNF- alpha) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF- alpha while cells that express CD8 secrete little or no TNF- alpha. Synthesis of TNF- alpha can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF- alpha has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF- alpha mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF- alpha that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF- alpha, which binds to both murine TNF receptors. Based on these results, many TNF- alpha mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF- alpha High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo.

Supplier: Prosci

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerization of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

Supplier: MilliporeSigma

Activates a variety of immune defense mechanisms by interactions with polymorphonuclear leukocytes, T cells, antibody-producing B lymphocytes, fibroblasts, and hematopoietic bone marrow cells. Activity is not species-specific. Induces apoptosis in human blood and bone marrow neutrophils and in endothelial cells. Increases iNOS levels in vascular smooth muscle cells. Involved in pathophysiological processes of several chronic and acute diseases. Stimulates stress activated protein (SAP) kinase. Biological activity: ED50=20–50pg/mL as measured in a cytotoxicity assay with the TNF-[alpha]-susceptible murine L-929 cells line in the presence of Actinomycin D (80055-066).

Supplier: Prosci

The Fas is also known as FAS receptor (FasR), apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs) are found in most mammals. Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor. This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain. Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.

Supplier: Thermo Scientific

HRP-Conjugated Streptavidin consists of streptavidin protein that is covalently conjugated to horseradish peroxidase (HRP) enzyme (RZ > 3.0). Streptavidin binds to biotin and the conjugated HRP provides enzyme activity for detection using an appropriate substrate system. This particular product has been used primarily in sandwich ELISA applications to provide consistent measurement of biotinylated detection antibodies.

Formulation: Provided in a conjugate stabilizer containing 0.1% ProClin Compound as a preservative.
Shipped on cold packs.
Application: ELISA: to be used with biotin-labeled detection antibodies. Recommended dilution range is from 1:4,000 to 1:20,000. The optimal dilution must be determined empirically for each specific application. Prepare dilutions immediately before use.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important homeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens. IL-2 promotes T cell proliferation and particularly naive T cells. IL-2 signaling on activated T cells is effected through a quaternary high-affinity receptor complex consisting of IL-2, IL-2Ralpha (CD25), IL-2Rbeta and IL-2Rgamma. Naive T cells are relatively insensitive to IL-2 as they only express small amounts of IL-2Rbeta and IL-2Rgamma. They only acquire sensitivity after CD25 expression, which captures the cytokine and presents it to the IL-2Rbeta and IL-2Rgamma receptors. IL-2 Superkine (Fc) is an artificial variant of IL-2 containing mutations at positions L80F / R81D / L85V / I 86V / I92F. These mutations are located in the molecule's core that acts to stabilize the structure and to give it a receptor-binding conformation mimicking native IL-2 bound to CD25. These mutations effectively eliminate the functional requirement of IL-2 for CD25 expression and elicit proliferation of T cells. Compared to IL-2, the IL-2 superkine induces superior expansion of cytotoxic T cells, leading to improved antitumour responses in vivo, and elicits proportionally less toxicity by lowering the expansion of Tregulatory cells and reducing pulmonary oedema.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

Receptors for the Fc region of immunoglobin G (Fc gamma R) are divided into three classes and Fc gamma RIII is a multifunctional, low/intermediate affinity receptor. In humans, Fc gamma RIII is expressed as two distinct forms (Fc gamma RIIIA and Fc gamma RIIIB) that are encoded by two different but highly homologous genes in a cell type-specific manner. Fc gamma RIIIB is a low-affinity, GPI-linked receptor expressed by neutrophils and eosinophils, whereas Fc gamma RIIIA is an intermediate affinity polypeptide-anchored transmembrane glycoprotein expressed by a subset of T lymphocytes, natural killer (NK) cells, monocytes, and macrophages. The Fc gamma RIIIA receptor is involved in phagocytosis, secretion of enzymes, inflammatory mediators, antibody-dependent cellular cytotoxicity (ADCC), mast cell degranulation, and clearance of immune complexes. Fc gamma RIIIA has an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain and delivers an activation signal in the immune responses. Aberrant expression or mutations in this gene is implicated in susceptibility to recurrent viral infections, systemic lupus erythematosus, and alloimmune neonatal neutropenia. In humans, it is a 50 -70 kD type I transmembrane activating receptor. The Fc gamma RIIIA cDNA encodes 254 amino acid including a 16aa signal sequence, 191 amino acid ECD with two C2-type Ig-like domains, five potential N-glycosylation sites, a 22 amino acid transmembrane sequence and a 25 amino acid cytoplasmic domain.

Supplier: Prosci

Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Human Fc gamma Rs are divided into three classes designated Fc gamma RI (CD64), Fc gamma RII (CD32), and Fc gamma RIII (CD16), which generate multiple isoforms, are recognized. The activating­ type receptor either has or associates non­covalently with an accessory subunit that has an immunoreceptor tyrosine­based activation motif (ITAM) in its cytoplasmic domain. Fc gamma RI binds IgG with high affinity and functions during early immune responses, whereas Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. Three genes for human Fc gamma RII (A, B, and C) and one for mouse (Fc gamma RIIB), encoding type I transmembrane proteins with ITAM motifs (Fc gamma RII A and C) or ITIM motifs (Fc gamma RIIB) in their cytoplasmic domains, have been identified. Human CD32, also known as Low affinity immunoglobulin gamma Fc region receptor II-a (IgG Fc receptor II-a), Fc gamma RII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcR gamma , CD32a (Fc gamma RII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fc gamma RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors.

Supplier: Prosci

Interleukin-20 (IL-20) is a member of the IL-10 family of regulatory cytokines that includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences but they are dissimilar in their biological functions. IL-20 exhibits approximately 28% amino acid identity with IL-10 and 76% amino acid identity with mouse IL-20. There are two heterodimeric receptor complexes for IL-20. The first is composed of IL-20 R alpha and IL-20 R beta . The second is composed of IL-22 R and IL-20 R beta . Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24, the IL-20 R alpha/IL-20 R beta complex is shared with both IL-19 and IL-24. IL-20 has been shown to initiate transduction cascades involving STAT3 and stimulates the induction of pro-inflammatory genes including TNF- alpha and MCP-1. Initial functional studies using transgenic mice suggest that IL-20 has the ability to regulate skin development. The over-expression of both human and mouse forms of IL-20 results in keratinocyte hyper-proliferation, abnormal epidermal differentiation, and neonatal lethality. In humans, IL-20 and its receptors are up-regulated in psoriatic skin, and polymorphisms in the IL-20 gene have been associated with plaque-type psoriasis. IL-20 may also have a role in hematopoiesis. It enhances the proliferation of multi-potential progenitors in vitro and increases their numbers and cell cycling status in IL-20 transgenic mice. IL-20 is also shown to suppress COX-2 and PGE2 and acts as an inhibitor of angiogenesis in model systems.

Supplier: Abnova

The Recombinant Human MTF2 Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human MTF2 Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: Abnova

The Recombinant Human HIST2H3A Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human HIST2H3A Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: Abnova

The Recombinant Human PKN3 Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human PKN3 Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: Abnova

Human ADAM5P full-length ORF (AAH67864.2, 1 a.a. to 412 a.a.) recombinant protein with GST-tag at N-terminal.

Supplier: New England Biolabs (NEB)

NEBExpress GamS nuclease inhibitor is a recombinant protein that inhibits Exonuclease V (RecBCD) activity and stabilizes linear DNA templates in E. coli based in vitro protein synthesis reactions.